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Protein

Signal peptidase complex subunit 3

Gene

SPCS3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Component of the microsomal signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease

Enzyme and pathway databases

ReactomeiR-HSA-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-HSA-381771. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
R-HSA-400511. Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP).
R-HSA-422085. Synthesis, secretion, and deacylation of Ghrelin.

Names & Taxonomyi

Protein namesi
Recommended name:
Signal peptidase complex subunit 3 (EC:3.4.-.-)
Alternative name(s):
Microsomal signal peptidase 22/23 kDa subunit
Short name:
SPC22/23
Short name:
SPase 22/23 kDa subunit
Gene namesi
Name:SPCS3
Synonyms:SPC22
ORF Names:UNQ1841/PRO3567
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:26212. SPCS3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1111CytoplasmicSequence analysisAdd
BLAST
Transmembranei12 – 3221Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini33 – 180148LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134910080.

Polymorphism and mutation databases

BioMutaiSPCS3.
DMDMi46577648.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 180180Signal peptidase complex subunit 3PRO_0000218938Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi141 – 1411N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiP61009.
MaxQBiP61009.
PaxDbiP61009.
PeptideAtlasiP61009.
PRIDEiP61009.
TopDownProteomicsiP61009.

PTM databases

iPTMnetiP61009.
PhosphoSiteiP61009.
SwissPalmiP61009.

Expressioni

Gene expression databases

BgeeiP61009.
CleanExiHS_SPCS3.
GenevisibleiP61009. HS.

Organism-specific databases

HPAiHPA053180.

Interactioni

Subunit structurei

Component of the microsomal signal peptidase complex which consists of five members: SEC11A, SEC11C, SPCS1, SPCS2 and SPCS3.By similarity

Protein-protein interaction databases

BioGridi121940. 12 interactions.
IntActiP61009. 9 interactions.
MINTiMINT-3022145.
STRINGi9606.ENSP00000427463.

Structurei

3D structure databases

ProteinModelPortaliP61009.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SPCS3 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3372. Eukaryota.
ENOG4110TZP. LUCA.
GeneTreeiENSGT00390000009223.
HOGENOMiHOG000246793.
HOVERGENiHBG054497.
InParanoidiP61009.
KOiK12948.
OMAiVDDFTGP.
OrthoDBiEOG773XHG.
PhylomeDBiP61009.
TreeFamiTF300185.

Family and domain databases

InterProiIPR007653. SPC22.
[Graphical view]
PANTHERiPTHR12804. PTHR12804. 1 hit.
PfamiPF04573. SPC22. 1 hit.
[Graphical view]
PIRSFiPIRSF016089. SPC22. 1 hit.

Sequencei

Sequence statusi: Complete.

P61009-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTVLSRANS LFAFSLSVMA ALTFGCFITT AFKDRSVPVR LHVSRIMLKN
60 70 80 90 100
VEDFTGPRER SDLGFITFDI TADLENIFDW NVKQLFLYLS AEYSTKNNAL
110 120 130 140 150
NQVVLWDKIV LRGDNPKLLL KDMKTKYFFF DDGNGLKGNR NVTLTLSWNV
160 170 180
VPNAGILPLV TGSGHVSVPF PDTYEITKSY
Length:180
Mass (Da):20,313
Last modified:April 26, 2004 - v1
Checksum:i342AB8E0F3F6D71A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 681F → S in CAB66595 (PubMed:11230166).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL136660 mRNA. Translation: CAB66595.1.
AK026302 mRNA. Translation: BAB15437.1.
AY359044 mRNA. Translation: AAQ89403.1.
BC047290 mRNA. Translation: AAH47290.1.
CCDSiCCDS54823.1.
RefSeqiNP_068747.1. NM_021928.3.
UniGeneiHs.42194.

Genome annotation databases

EnsembliENST00000503362; ENSP00000427463; ENSG00000129128.
GeneIDi60559.
KEGGihsa:60559.
UCSCiuc003iur.5. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL136660 mRNA. Translation: CAB66595.1.
AK026302 mRNA. Translation: BAB15437.1.
AY359044 mRNA. Translation: AAQ89403.1.
BC047290 mRNA. Translation: AAH47290.1.
CCDSiCCDS54823.1.
RefSeqiNP_068747.1. NM_021928.3.
UniGeneiHs.42194.

3D structure databases

ProteinModelPortaliP61009.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121940. 12 interactions.
IntActiP61009. 9 interactions.
MINTiMINT-3022145.
STRINGi9606.ENSP00000427463.

PTM databases

iPTMnetiP61009.
PhosphoSiteiP61009.
SwissPalmiP61009.

Polymorphism and mutation databases

BioMutaiSPCS3.
DMDMi46577648.

Proteomic databases

EPDiP61009.
MaxQBiP61009.
PaxDbiP61009.
PeptideAtlasiP61009.
PRIDEiP61009.
TopDownProteomicsiP61009.

Protocols and materials databases

DNASUi60559.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000503362; ENSP00000427463; ENSG00000129128.
GeneIDi60559.
KEGGihsa:60559.
UCSCiuc003iur.5. human.

Organism-specific databases

CTDi60559.
GeneCardsiSPCS3.
H-InvDBHIX0200687.
HGNCiHGNC:26212. SPCS3.
HPAiHPA053180.
neXtProtiNX_P61009.
PharmGKBiPA134910080.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3372. Eukaryota.
ENOG4110TZP. LUCA.
GeneTreeiENSGT00390000009223.
HOGENOMiHOG000246793.
HOVERGENiHBG054497.
InParanoidiP61009.
KOiK12948.
OMAiVDDFTGP.
OrthoDBiEOG773XHG.
PhylomeDBiP61009.
TreeFamiTF300185.

Enzyme and pathway databases

ReactomeiR-HSA-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-HSA-381771. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
R-HSA-400511. Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP).
R-HSA-422085. Synthesis, secretion, and deacylation of Ghrelin.

Miscellaneous databases

ChiTaRSiSPCS3. human.
GenomeRNAii60559.
PROiP61009.

Gene expression databases

BgeeiP61009.
CleanExiHS_SPCS3.
GenevisibleiP61009. HS.

Family and domain databases

InterProiIPR007653. SPC22.
[Graphical view]
PANTHERiPTHR12804. PTHR12804. 1 hit.
PfamiPF04573. SPC22. 1 hit.
[Graphical view]
PIRSFiPIRSF016089. SPC22. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Small intestine.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pancreas.
  5. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-141.
    Tissue: Liver.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSPCS3_HUMAN
AccessioniPrimary (citable) accession number: P61009
Secondary accession number(s): P12280, Q9H0S7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: July 6, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.